Inhibition of Glycation-Induced Aggregation of Human Serum Albumin by Organic–Inorganic Hybrid Nanocomposites of Iron Oxide-Functionalized Nanocellulose
| Autor: | Aqib Iqbal Dar, Rubbel Singla, Amitabha Acharya, Syed M. S. Abidi |
|---|---|
| Rok vydání: | 2019 |
| Předmět: | |
| Zdroj: | ACS Omega ACS Omega, Vol 4, Iss 12, Pp 14805-14819 (2019) |
| ISSN: | 2470-1343 |
| Popis: | Protein aggregation leads to the transformation of proteins from their soluble form to the insoluble amyloid fibrils and these aggregates get deposited in the specific body tissues, accounting for various diseases. To prevent such an aggregation, organic–inorganic hybrid nanocomposites of iron oxide nanoparticle (NP, ∼6.5–7.0 nm)-conjugated cellulose nanocrystals (CNCs) isolated from Syzygium cumini (SC) and Pinus roxburghii (PR) were chemically synthesized. Transmission electron microscopy (TEM) images of the nanocomposites suggested that the in situ-synthesized iron oxide NPs were bound to the CNC surface in a uniform and regular fashion. The ThT fluorescence assay together with 8-anilino-1-naphthalenesulfonic acid, Congo Red, and CD studies suggested that short fiber-based SC nanocomposites showed better inhibition as well as dissociation of human serum albumin aggregates. The TEM and fluorescence microscopy studies supported similar observations. Native polyacrylamide gel electrophoresis results documented dissociation of higher protein aggregates in the presence of the developed nanocomposite. Interestingly, the dissociated proteins retained their biological function by maintaining a high amount of α-helix content. The in vitro studies with HEK-293 cells suggested that the developed nanocomposite reduces aggregation-induced cytotoxicity by intracellular reactive oxygen species scavenging and maintaining the Ca2+ ion-channel. These results indicated that the hybrid organic–inorganic nanocomposite, with simultaneous sites for hydrophobic and hydrophilic interactions, tends to provide a larger surface area for nanocomposite–protein interactions, which ultimately disfavors the nucleation step for fibrillation for protein aggregates. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|